Date published: 2025-9-15

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RBMS2 Inhibitors

Chemical inhibitors of RBMS2 can exert their inhibitory effects through a variety of biochemical and cellular mechanisms. Staurosporine, a kinase inhibitor, can disrupt key signaling pathways that are essential for RBMS2's function in RNA binding and modulation. By inhibiting these kinases, staurosporine can alter the phosphorylation state of proteins that interact with RBMS2 or are involved in its regulation. LY294002 and rapamycin target the PI3K/AKT/mTOR pathway, which is integral to cellular growth and metabolism. LY294002 directly inhibits PI3K, which can attenuate AKT signaling and indirectly affect RBMS2's activity. Rapamycin, by inhibiting mTOR, can decrease the phosphorylation of downstream proteins that may interact with RBMS2, thereby inhibiting its function.

Spliceostatin A and pladienolide B specifically target the splicing machinery, which is closely related to the function of RBMS2 in RNA processing. By inhibiting the splicing of pre-mRNAs that RBMS2 binds, spliceostatin A can functionally inhibit RBMS2. Similarly, pladienolide B disrupts the spliceosome function, which can lead to a functional inhibition of RBMS2's RNA-binding activity. MEK inhibitors like U0126 and PD98059 can impair the ERK signaling pathway, which may regulate processes essential for RBMS2's activity; thus, inhibiting MEK can lead to an inhibition of RBMS2. Leflunomide, by inhibiting pyrimidine synthesis, can influence the availability of RNA substrates that RBMS2 would typically bind, thereby inhibiting its function. 5-Azacytidine, which incorporates into RNA, can interfere with RNA-protein interactions, directly inhibiting RBMS2's ability to bind its RNA targets. Triptolide disrupts transcriptional processes, which indirectly inhibits RBMS2 by reducing the RNA available for binding. Flavopiridol inhibits CDKs, affecting transcription regulation and cell cycle progression, which can inhibit RBMS2's role in RNA processing. Lastly, Actinomycin D intercalates into DNA, inhibiting transcription, thus reducing the RNA substrate pool essential for RBMS2's interaction and function.

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